IL-1R2 Protein, Rat (HEK293, His)

IL-1R2 is a competitive endogenous inhibitor of IL-1 signaling. IL-1R2 serves as a decoy receptor and competes with IL-1R1 for IL-1, it can also form a complex with IL-1RAP once it binds IL-1. IL-1R2 is implicated in various IL-1-mediated inflammatory diseases^[1]. IL-1R2 Protein, Rat (HEK293, His) is a recombinant rat IL-1R2 protein with a His tag at the C-terminus and is expressed in HEK293 cells. It consists of 355 amino acids (M1-E355).

IL-1R2 is the non-signaling type 2 interleukin-1 receptor and is natively found on neutrophils, B-cells, monocytes and macrophages. The rat IL-1R2 can be cleaved into two forms: membrane form (14-416 a.a) and soluble form (14-? a.a).
The sequence of amino acids in IL-1R2 from rat shows low similarity (about 60%) with human IL-1R2, but has been only slightly altered with mouse IL-1R2 (90 % similarity).
IL-1R2 contains truncated cytoplasmic domain and lacks Toll-IL-1 receptor (TIR) region, making it incapable of transmembrane signaling. IL-1R2 serves as an endogenous inhibitor of IL-1 signaling. Functional IL-1 signaling requires IL-1R1 and IL-1-dependent recruitment of IL-1RAP. IL-1R2 serves as a decoy receptor and can compete with IL-1R1 for IL-1. IL-1R2 can also form a complex with IL-1RAP once it binds IL-1, preventing IL-1RAP from heterodimerizing with IL-1R1. Through these 2 ways, IL-1R2 blocks IL-1 signaling. Additionally, soluble IL-1R2 recruits soluble IL-1RAP with high affinity without impacting affinity for IL-1RA.
IL-1R2 inhibits IL-1 signaling and has been implicated in various IL-1-mediated inflammatory diseases like arthritis, diabetes, gout and so on^[1][2][3].

IL-1R2 (8 μg of pCAGGS-IL-1RII-IgGFc; tail vein; once) inhibits IL-1-induced immune responses in Lewis rats^[4].

Measured by its binding ability in a functional ELISA. Immobilized Rat IL-1R2 at 2 μg/mL (100 μL/well) can bind biotinylated Human IL-1 beta. The ED₅₀ for this effect is 19.20 ng/mL.

Rat

HEK293

C-6*His

P43303 (F14-E355)

117022  [NCBI]

FTTPAVVHTGRVSESPVTSEKHPVLGDDCWFRGRDFKSELRLEGEPVVLRCPLVPHSDTSSSSRSLLTWSKSDSSQLIPGDEPRMWVKDDTLWVLPAVQQDSGTYICTFRNASHCEQMSLELKVFKNTEASFPLVSYLQISALSSTGLLVCPDLKEFISSRTDGKIQWYKGSILLDKGNKKFLSAGDPTRLLISNTSMGDAGYYRCVMTFTYEGKEYNITRNIELRVKGITTEPIPVIISPLETIPASLGSRLIVPCKVFLGTGTSSNTIVWWMANSTFISVAYPRGRVTEGLHHQYSENDENYVEVSLIFDPVTKEDLNTDFKCVATNPRSFQSLHTTVKE

Approximately 50-60 kDa due to the glycosylation

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. PetersVA,etal.IL-1receptor2(IL-1R2)anditsroleinimmuneregulation.BrainBehavImmun.2013Aug;32:1-8.  [Content Brief]

  [2]. Molgora M, et al. Tuning inflammation and immunity by the negative regulators IL-1R2 and IL-1R8. Immunol Rev. 2018 Jan;281(1):233-247.  [Content Brief]

  [3]. Lin J, et al. Cardiomyocyte IL-1R2 protects heart from ischemia/reperfusion injury by attenuating IL-17RA-mediated cardiomyocyte apoptosis. Cell Death Dis. 2022 Jan 27;13(1):90.  [Content Brief]

  [4]. Chang H, et al. Hydrodynamics-based delivery of an interleukin-1 receptor II fusion gene ameliorates rat autoimmune myocarditis by inhibiting IL-1 and Th17 cell polarization. Int J Mol Med. 2013 Apr;31(4):833-40.  [Content Brief]